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1MHE.pdb
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1MHE.pdb
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HEADER MAJOR HISTOCOMPATIBILITY COMPLEX 24-AUG-98 1MHE
TITLE THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX
TITLE 2 MOLECULE HLA-E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN HLA-E;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, ALPHA CHAIN E;
COMPND 5 SYNONYM: MHC NONCLASSICAL CHAIN, MHC-E, HLA-E, MHC CLASS
COMPND 6 IB, MHC CLASS 1B;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B, D;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: PEPTIDE (VMAPRTVLL);
COMPND 14 CHAIN: P, Q;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: PEPTIDE SEQUENCE IS THAT OF THE LEADER
COMPND 17 SEQUENCE OF THE CLASSICAL CLASS I MOLECULES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: HLA-E;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODIES;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: COC057;
SOURCE 12 OTHER_DETAILS: DENATURED AND REFOLDED IN THE PRESENCE OF
SOURCE 13 PEPTIDE AND BETA-2-MICROGLOBULIN;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 CELL_LINE: BL21;
SOURCE 19 GENE: BETA-2-MICROGLOBULIN;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: XA 90;
SOURCE 23 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODIES;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PHN1;
SOURCE 25 MOL_ID: 3
KEYWDS HLA-E, HLA E, MAJOR HISTOCOMPATIBILITY COMPLEX, MHC, HLA,
KEYWDS 2 BETA 2 MICROGLOBULIN, PEPTIDE, LEADER PEPTIDE, NON-
KEYWDS 3 CLASSICAL MHC, CLASS IB MHC
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.O'CALLAGHAN,J.TORMO,B.E.WILLCOX,V.B.BRAUD,B.K.JAKOBSEN,
AUTHOR 2 D.I.STUART,A.J.MCMICHAEL,J.I.BELL,E.Y.JONES
REVDAT 3 24-FEB-09 1MHE 1 VERSN
REVDAT 2 01-APR-03 1MHE 1 JRNL
REVDAT 1 23-MAR-99 1MHE 0
JRNL AUTH C.A.O'CALLAGHAN,J.TORMO,B.E.WILLCOX,V.M.BRAUD,
JRNL AUTH 2 B.K.JAKOBSEN,D.I.STUART,A.J.MCMICHAEL,J.I.BELL,
JRNL AUTH 3 E.Y.JONES
JRNL TITL STRUCTURAL FEATURES IMPOSE TIGHT PEPTIDE BINDING
JRNL TITL 2 SPECIFICITY IN THE NONCLASSICAL MHC MOLECULE HLA-E.
JRNL REF MOL.CELL V. 1 531 1998
JRNL REFN ISSN 1097-2765
JRNL PMID 9660937
JRNL DOI 10.1016/S1097-2765(00)80053-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.A.O'CALLAGHAN,J.TORMO,B.E.WILLCOX,C.D.BLUNDELL,
REMARK 1 AUTH 2 B.K.JAKOBSEN,D.I.STUART,A.J.MCMICHAEL,J.I.BELL,
REMARK 1 AUTH 3 E.Y.JONES
REMARK 1 TITL PRODUCTION, CRYSTALLIZATION, AND PRELIMINARY X-RAY
REMARK 1 TITL 2 ANALYSIS OF THE HUMAN MHC CLASS IB MOLECULE HLA-E
REMARK 1 REF PROTEIN SCI. V. 7 1264 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 35977
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2716
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.10
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4147
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 310
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6608
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.57
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.62
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.55
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.13
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TOPPAR:PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : SO4.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : SO4.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IT SHOULD BE NOTED THAT THE
REMARK 3 APPLICATION OF OVERALL ANISOTROPIC B SCALING LED TO A
REMARK 3 SIGNIFICANT INCREASE OF THE TEMPERATURE FACTORS.
REMARK 4
REMARK 4 1MHE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR 1 AND MIRROR 2
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37611
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.48300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 3HLA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.46667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.93333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.93333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.46667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, P, Q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1 HLA-E*0101
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1mhe_A,1mhe_B
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1 HLA-E*0101
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1mhe_C,1mhe_D
REMARK 410
REMARK 410 ligand(s)
REMARK 410 MH1 HLA-B*0714 peptide (HLA01049)
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1mhe_Q
REMARK 410
REMARK 410 ligand(s)
REMARK 410 MH1 HLA-B*0714 peptide (HLA01049)
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Homo sapiens (human)
REMARK 410 Chain ID
REMARK 410 1mhe_P
REMARK 410
REMARK 410
REMARK 410 Chain ID 1mhe_A (1MHEA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-89) [D1]
REMARK 410 GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRS
REMARK 410 ][ G-ALPHA
REMARK 410 ARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDRRFLRGYEQFAYDGKDYLTLNEDLRS
REMARK 410 2 (90-181) [D2] ][
REMARK 410 WTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHE
REMARK 410 C-LIKE (182-273) [D3]
REMARK 410 ATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHE
REMARK 410 ]
REMARK 410 GLPEPVTLRW
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHSLKY.FHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAA
REMARK 410 G-DOMAIN SPRMVPRA.......PWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYN
REMARK 410 G-DOMAIN QSEA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTLQWMHGCELGPDRRFLRGYEQFAYDGKDYLTLNED..L
REMARK 410 G-DOMAIN RSWTAVD.......TAAQISEQKSNDA.SEAEHQRAYLEDTCVEWLHKYLEK
REMARK 410 G-DOMAIN GKETLLHL
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......EPPKTHVTHHPISD......HEATLRCWALGFYP..AEITLTWQQ
REMARK 410 C-LIKE-DOMAIN DGEGHTQ..DTELVETRPAGD......GTFQKWAAVVVPSG.....EEQRYT
REMARK 410 C-LIKE-DOMAIN CHVQHEG..LPEPVTLRW
REMARK 410
REMARK 410 Chain ID 1mhe_B (1MHEB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLL
REMARK 410 ]
REMARK 410 YYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens B2M*01
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele B2M*02 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQRTPKIQVYSRHPAEN....GKSNFLNCYVSGFHP..SDIEVDLLK
REMARK 410 C-LIKE-DOMAIN NGERIE...KVEHSDLSFSKD......WSFYLLYYTEFTPTE.....KDEYA
REMARK 410 C-LIKE-DOMAIN CRVNHVT..LSQPKIVKWDRDM
REMARK 410
REMARK 410 Chain ID 1mhe_C (1MHEC)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-89) [D1]
REMARK 410 GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRS
REMARK 410 ][ G-ALPHA
REMARK 410 ARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDRRFLRGYEQFAYDGKDYLTLNEDLRS
REMARK 410 2 (90-181) [D2] ][
REMARK 410 WTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHE
REMARK 410 C-LIKE (182-273) [D3]
REMARK 410 ATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHE
REMARK 410 ]
REMARK 410 GLPEPVTLRW
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHSLKY.FHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAA
REMARK 410 G-DOMAIN SPRMVPRA.......PWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYN
REMARK 410 G-DOMAIN QSEA
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTLQWMHGCELGPDRRFLRGYEQFAYDGKDYLTLNED..L
REMARK 410 G-DOMAIN RSWTAVD.......TAAQISEQKSNDA.SEAEHQRAYLEDTCVEWLHKYLEK
REMARK 410 G-DOMAIN GKETLLHL
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens HLA-E*0101
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......EPPKTHVTHHPISD......HEATLRCWALGFYP..AEITLTWQQ
REMARK 410 C-LIKE-DOMAIN DGEGHTQ..DTELVETRPAGD......GTFQKWAAVVVPSG.....EEQRYT
REMARK 410 C-LIKE-DOMAIN CHVQHEG..LPEPVTLRW
REMARK 410
REMARK 410 Chain ID 1mhe_D (1MHED)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLL
REMARK 410 ]
REMARK 410 YYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Homo sapiens B2M*01
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%), Homo sapiens
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele B2M*02 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQRTPKIQVYSRHPAEN....GKSNFLNCYVSGFHP..SDIEVDLLK
REMARK 410 C-LIKE-DOMAIN NGERIE...KVEHSDLSFSKD......WSFYLLYYTEFTPTE.....KDEYA
REMARK 410 C-LIKE-DOMAIN CRVNHVT..LSQPKIVKWDRDM
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 GLY C 1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 480 GLY A 223 N CA C O
REMARK 480 HIS A 224 N CA C O CB CG ND1
REMARK 480 HIS A 224 CD2 CE1 NE2
REMARK 480 THR A 225 N CA C O CB OG1 CG2
REMARK 480 GLN A 226 N CA C O CB CG CD
REMARK 480 GLN A 226 OE1 NE2
REMARK 480 ASP A 227 N CA C O CB CG OD1
REMARK 480 ASP A 227 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 35 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 131 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 131 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG C 35 CG - CD - NE ANGL. DEV. = -18.0 DEGREES
REMARK 500 ARG C 35 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG C 35 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG C 35 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG C 44 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 44 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG C 48 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG C 48 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 65 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG C 65 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG C 108 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG C 108 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG C 108 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG C 131 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 131 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 202 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 202 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG C 234 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 45 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG D 45 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 17 24.26 -74.80
REMARK 500 ASP A 29 -123.52 55.54
REMARK 500 TRP A 51 2.73 -64.43
REMARK 500 ASN A 77 -37.72 -39.99
REMARK 500 ASP A 106 2.32 -66.89
REMARK 500 LEU A 110 -59.59 -121.85
REMARK 500 GLU A 114 139.72 -174.30
REMARK 500 ASP A 119 50.21 34.67
REMARK 500 TYR A 123 -70.07 -116.60
REMARK 500 ASP A 137 124.20 170.74
REMARK 500 THR A 138 -5.76 -53.97
REMARK 500 ASP A 162 -78.00 -106.73
REMARK 500 HIS A 188 154.84 165.56
REMARK 500 TYR A 209 136.97 -171.68
REMARK 500 ASP A 220 47.66 38.19
REMARK 500 GLU A 222 175.78 -53.37
REMARK 500 THR A 225 34.71 169.56
REMARK 500 GLN A 226 57.10 -91.19
REMARK 500 ASP A 227 20.85 134.24
REMARK 500 PRO A 269 164.63 -48.63
REMARK 500 ARG A 273 -32.70 -150.19
REMARK 500 TRP B 60 -3.08 71.57
REMARK 500 ARG C 17 3.18 -64.69
REMARK 500 ASP C 29 -123.13 55.21
REMARK 500 TRP C 51 2.79 -64.21
REMARK 500 ASP C 106 1.93 -67.74
REMARK 500 LEU C 110 -58.83 -120.20
REMARK 500 GLU C 114 139.90 -173.56
REMARK 500 ASP C 119 50.40 39.58
REMARK 500 ASP C 137 158.84 168.39
REMARK 500 ASP C 162 -78.78 -107.14
REMARK 500 HIS C 188 155.16 167.98
REMARK 500 ILE C 194 -64.25 -101.69
REMARK 500 TYR C 209 137.70 -171.09
REMARK 500 THR C 225 -25.10 -158.73
REMARK 500 GLN C 226 72.15 -62.70
REMARK 500 ASP C 227 21.48 118.10
REMARK 500 PRO C 269 166.07 -48.08
REMARK 500 TRP D 60 -4.90 67.92
REMARK 500 THR Q 6 -152.50 -80.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 35 0.13 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
DBREF 1MHE A 1 274 UNP P13747 HLAE_HUMAN 22 295
DBREF 1MHE B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 1MHE C 1 274 UNP P13747 HLAE_HUMAN 22 295
DBREF 1MHE D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 1MHE P 1 9 PDB 1MHE 1MHE 1 9
DBREF 1MHE Q 1 9 PDB 1MHE 1MHE 1 9
SEQRES 1 A 274 GLY SER HIS SER LEU LYS TYR PHE HIS THR SER VAL SER
SEQRES 2 A 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY
SEQRES 3 A 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP ASN ASP
SEQRES 4 A 274 ALA ALA SER PRO ARG MET VAL PRO ARG ALA PRO TRP MET
SEQRES 5 A 274 GLU GLN GLU GLY SER GLU TYR TRP ASP ARG GLU THR ARG
SEQRES 6 A 274 SER ALA ARG ASP THR ALA GLN ILE PHE ARG VAL ASN LEU
SEQRES 7 A 274 ARG THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 274 SER HIS THR LEU GLN TRP MET HIS GLY CYS GLU LEU GLY
SEQRES 9 A 274 PRO ASP ARG ARG PHE LEU ARG GLY TYR GLU GLN PHE ALA
SEQRES 10 A 274 TYR ASP GLY LYS ASP TYR LEU THR LEU ASN GLU ASP LEU
SEQRES 11 A 274 ARG SER TRP THR ALA VAL ASP THR ALA ALA GLN ILE SER
SEQRES 12 A 274 GLU GLN LYS SER ASN ASP ALA SER GLU ALA GLU HIS GLN
SEQRES 13 A 274 ARG ALA TYR LEU GLU ASP THR CYS VAL GLU TRP LEU HIS
SEQRES 14 A 274 LYS TYR LEU GLU LYS GLY LYS GLU THR LEU LEU HIS LEU
SEQRES 15 A 274 GLU PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER
SEQRES 16 A 274 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN GLN ASP GLY
SEQRES 18 A 274 GLU GLY HIS THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 274 VAL GLN HIS GLU GLY LEU PRO GLU PRO VAL THR LEU ARG
SEQRES 22 A 274 TRP
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 274 GLY SER HIS SER LEU LYS TYR PHE HIS THR SER VAL SER
SEQRES 2 C 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY
SEQRES 3 C 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP ASN ASP
SEQRES 4 C 274 ALA ALA SER PRO ARG MET VAL PRO ARG ALA PRO TRP MET
SEQRES 5 C 274 GLU GLN GLU GLY SER GLU TYR TRP ASP ARG GLU THR ARG
SEQRES 6 C 274 SER ALA ARG ASP THR ALA GLN ILE PHE ARG VAL ASN LEU
SEQRES 7 C 274 ARG THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 C 274 SER HIS THR LEU GLN TRP MET HIS GLY CYS GLU LEU GLY
SEQRES 9 C 274 PRO ASP ARG ARG PHE LEU ARG GLY TYR GLU GLN PHE ALA
SEQRES 10 C 274 TYR ASP GLY LYS ASP TYR LEU THR LEU ASN GLU ASP LEU
SEQRES 11 C 274 ARG SER TRP THR ALA VAL ASP THR ALA ALA GLN ILE SER
SEQRES 12 C 274 GLU GLN LYS SER ASN ASP ALA SER GLU ALA GLU HIS GLN
SEQRES 13 C 274 ARG ALA TYR LEU GLU ASP THR CYS VAL GLU TRP LEU HIS
SEQRES 14 C 274 LYS TYR LEU GLU LYS GLY LYS GLU THR LEU LEU HIS LEU
SEQRES 15 C 274 GLU PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER
SEQRES 16 C 274 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 C 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN GLN ASP GLY
SEQRES 18 C 274 GLU GLY HIS THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 C 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 C 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS
SEQRES 21 C 274 VAL GLN HIS GLU GLY LEU PRO GLU PRO VAL THR LEU ARG
SEQRES 22 C 274 TRP
SEQRES 1 D 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 P 9 VAL MET ALA PRO ARG THR VAL LEU LEU
SEQRES 1 Q 9 VAL MET ALA PRO ARG THR VAL LEU LEU
HET SO4 1 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *8(H2 O)
HELIX 1 1 PRO A 50 MET A 52 5 3
HELIX 2 2 SER A 57 TYR A 85 1 29
HELIX 3 3 GLN A 1053 ALA A 1061A 1 10
HELIX 4 4 GLU A 1063 GLU A 1072 1 10
HELIX 5 5 THR A 1073 LYS A 1084 1 12
HELIX 6 6 LYS A 1086 LEU A 1089 1 4
HELIX 7 7 GLU A 2099 ARG A 2101 5 3
HELIX 8 8 PRO C 50 MET C 52 5 3
HELIX 9 9 SER C 57 TYR C 85 1 29
HELIX 10 10 ALA C 1052 ALA C 1061A 1 11
HELIX 11 11 GLU C 1063 GLU C 1072 1 10
HELIX 12 12 THR C 1073 LYS C 1084 1 12
HELIX 13 13 LYS C 1086 LEU C 1089 1 4
HELIX 14 14 GLU C 2099 ARG C 2101 5 3
SHEET 1 A 7 THR A 31 ASP A 37 0
SHEET 2 A 7 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31
SHEET 3 A 7 HIS A 3 VAL A 12 -1 N VAL A 12 O ARG A 21
SHEET 4 A 7 THR A1004 LEU A1013 -1 N LEU A1013 O HIS A 3
SHEET 5 A 7 PHE A1019 TYR A1028 -1 N ALA A1027 O GLN A1006
SHEET 6 A 7 LYS A1031 LEU A1036 -1 N LEU A1034 O PHE A1026
SHEET 7 A 7 TRP A1045 ALA A1047 -1 N THR A1046 O THR A1035
SHEET 1 B 3 LYS A2003 PRO A2010 0
SHEET 2 B 3 GLU A2018 LEU A2026 -1 N LEU A2026 O LYS A2003
SHEET 3 B 3 LYS A2085 PRO A2092 -1 N VAL A2091 O ALA A2019
SHEET 1 C 3 THR A2038 GLN A2043 0
SHEET 2 C 3 TYR A2102 GLN A2107 -1 N GLN A2107 O THR A2038
SHEET 3 C 3 VAL A2117 LEU A2119 -1 N LEU A2119 O CYS A2104
SHEET 1 D 3 LYS B1003 SER B1008 0
SHEET 2 D 3 SER B1018 PHE B1028 -1 N SER B1026 O LYS B1003
SHEET 3 D 3 PHE B1085B THR B1092 -1 N PHE B1091 O ASN B1019
SHEET 1 E 3 GLU B1038 LYS B1043 0
SHEET 2 E 3 TYR B1102 ASN B1107 -1 N ASN B1107 O GLU B1038
SHEET 3 E 3 LYS B1117 LYS B1120 -1 N VAL B1119 O CYS B1104
SHEET 1 F 7 THR C 31 ASP C 37 0
SHEET 2 F 7 ARG C 21 VAL C 28 -1 N VAL C 28 O THR C 31
SHEET 3 F 7 HIS C 3 VAL C 12 -1 N VAL C 12 O ARG C 21
SHEET 4 F 7 THR C1004 LEU C1013 -1 N LEU C1013 O HIS C 3
SHEET 5 F 7 PHE C1019 TYR C1028 -1 N ALA C1027 O GLN C1006
SHEET 6 F 7 LYS C1031 LEU C1036 -1 N LEU C1034 O PHE C1026
SHEET 7 F 7 TRP C1045 ALA C1047 -1 N THR C1046 O THR C1035
SHEET 1 G 4 LYS C2003 PRO C2010 0
SHEET 2 G 4 GLU C2018 LEU C2026 -1 N LEU C2026 O LYS C2003
SHEET 3 G 4 LYS C2085 PRO C2092 -1 N VAL C2091 O ALA C2019
SHEET 4 G 4 THR C2078 LEU C2080 -1 N GLU C2079 O ALA C2088
SHEET 1 H 3 THR C2038 GLN C2043 0
SHEET 2 H 3 TYR C2102 GLN C2107 -1 N GLN C2107 O THR C2038
SHEET 3 H 3 VAL C2117 ARG C2120 -1 N LEU C2119 O CYS C2104
SHEET 1 I 3 VAL D1006 SER D1008 0
SHEET 2 I 3 SER D1018 PHE D1028 -1 N ASN D1022 O TYR D1007
SHEET 3 I 3 PHE D1085B THR D1092 -1 N PHE D1091 O ASN D1019
SHEET 1 J 3 GLU D1038 LYS D1043 0
SHEET 2 J 3 TYR D1102 ASN D1107 -1 N ASN D1107 O GLU D1038
SHEET 3 J 3 LYS D1117 LYS D1120 -1 N VAL D1119 O CYS D1104
SSBOND 1 CYS A 1011 CYS A 1074 1555 1555
SSBOND 2 CYS A 2023 CYS A 2104 1555 1555
SSBOND 3 CYS B 1023 CYS B 1104 1555 1555
SSBOND 4 CYS C 1011 CYS C 1074 1555 1555
SSBOND 5 CYS C 2023 CYS C 2104 1555 1555
SSBOND 6 CYS D 1023 CYS D 1104 1555 1555
CISPEP 1 TYR A 2029 PRO A 2030 0 -0.30
CISPEP 2 HIS B 1029 PRO B 1030 0 -0.32
CISPEP 3 TYR C 2029 PRO C 2030 0 -0.81
CISPEP 4 HIS D 1029 PRO D 1030 0 1.01
SITE 1 AC1 1 ARG A 75
CRYST1 182.200 182.200 88.400 90.00 90.00 120.00 P 31 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005488 0.003169 0.000000 0.00000
SCALE2 0.000000 0.006338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011312 0.00000
ATOM 1 N SER A 1 107.703 -4.128 23.066 1.00 83.59 N
ATOM 2 CA SER A 1 107.189 -5.010 21.971 1.00 82.87 C
ATOM 3 C SER A 1 107.095 -4.258 20.644 1.00 83.23 C
ATOM 4 O SER A 1 106.477 -3.194 20.565 1.00 86.64 O
ATOM 5 CB SER A 1 105.814 -5.575 22.338 1.00 79.17 C
ATOM 6 OG SER A 1 105.271 -6.324 21.261 1.00 72.61 O
ATOM 7 HG SER A 1 104.420 -6.692 21.505 1.00 0.00 H
ATOM 8 N HIS A 2 107.728 -4.804 19.609 1.00 79.83 N
ATOM 9 CA HIS A 2 107.704 -4.192 18.284 1.00 75.37 C
ATOM 10 C HIS A 2 107.449 -5.255 17.230 1.00 72.76 C
ATOM 11 O HIS A 2 107.509 -6.458 17.514 1.00 74.35 O
ATOM 12 CB HIS A 2 109.021 -3.475 17.999 1.00 75.33 C
ATOM 13 CG HIS A 2 109.333 -2.410 18.992 1.00 76.39 C
ATOM 14 ND1 HIS A 2 108.538 -1.299 19.156 1.00 76.36 N
ATOM 15 CD2 HIS A 2 110.315 -2.312 19.918 1.00 78.65 C
ATOM 16 CE1 HIS A 2 109.014 -0.561 20.143 1.00 77.03 C
ATOM 17 NE2 HIS A 2 110.091 -1.155 20.623 1.00 79.15 N
ATOM 18 H HIS A 2 108.239 -5.635 19.732 1.00 0.00 H
ATOM 19 HD1 HIS A 2 107.729 -1.099 18.656 1.00 0.00 H
ATOM 20 HE2 HIS A 2 110.638 -0.824 21.370 1.00 0.00 H
ATOM 21 N SER A 3 107.214 -4.822 16.000 1.00 65.88 N
ATOM 22 CA SER A 3 106.939 -5.774 14.954 1.00 58.65 C
ATOM 23 C SER A 3 107.215 -5.220 13.585 1.00 54.68 C
ATOM 24 O SER A 3 107.168 -4.011 13.360 1.00 57.15 O
ATOM 25 CB SER A 3 105.477 -6.165 15.024 1.00 60.28 C
ATOM 26 OG SER A 3 104.685 -4.993 14.923 1.00 61.79 O
ATOM 27 H SER A 3 107.254 -3.865 15.803 1.00 0.00 H
ATOM 28 HG SER A 3 103.764 -5.252 15.015 1.00 0.00 H
ATOM 29 N LEU A 4 107.451 -6.133 12.658 1.00 49.14 N
ATOM 30 CA LEU A 4 107.708 -5.788 11.269 1.00 47.18 C
ATOM 31 C LEU A 4 106.743 -6.658 10.481 1.00 48.30 C
ATOM 32 O LEU A 4 106.838 -7.889 10.524 1.00 50.88 O
ATOM 33 CB LEU A 4 109.138 -6.155 10.907 1.00 45.75 C
ATOM 34 CG LEU A 4 109.518 -6.185 9.429 1.00 42.87 C
ATOM 35 CD1 LEU A 4 109.377 -4.816 8.782 1.00 44.21 C
ATOM 36 CD2 LEU A 4 110.959 -6.640 9.350 1.00 44.66 C
ATOM 37 H LEU A 4 107.458 -7.076 12.939 1.00 0.00 H
ATOM 38 N LYS A 5 105.821 -6.043 9.753 1.00 45.39 N
ATOM 39 CA LYS A 5 104.854 -6.830 9.016 1.00 42.12 C
ATOM 40 C LYS A 5 104.465 -6.255 7.684 1.00 41.13 C
ATOM 41 O LYS A 5 104.453 -5.043 7.506 1.00 46.17 O
ATOM 42 CB LYS A 5 103.622 -7.064 9.875 1.00 44.58 C
ATOM 43 CG LYS A 5 103.279 -5.926 10.819 1.00 51.44 C
ATOM 44 CD LYS A 5 102.175 -6.343 11.815 1.00 59.96 C
ATOM 45 CE LYS A 5 102.005 -5.346 12.991 1.00 66.31 C
ATOM 46 NZ LYS A 5 101.631 -3.927 12.615 1.00 71.56 N
ATOM 47 H LYS A 5 105.820 -5.070 9.682 1.00 0.00 H
ATOM 48 HZ1 LYS A 5 100.744 -3.965 12.065 1.00 0.00 H
ATOM 49 HZ2 LYS A 5 101.502 -3.334 13.465 1.00 0.00 H
ATOM 50 HZ3 LYS A 5 102.381 -3.518 12.013 1.00 0.00 H
ATOM 51 N TYR A 6 104.171 -7.133 6.734 1.00 38.92 N
ATOM 52 CA TYR A 6 103.784 -6.705 5.402 1.00 37.53 C
ATOM 53 C TYR A 6 102.394 -7.191 5.075 1.00 36.39 C
ATOM 54 O TYR A 6 101.875 -8.083 5.733 1.00 34.85 O
ATOM 55 CB TYR A 6 104.743 -7.266 4.374 1.00 38.03 C
ATOM 56 CG TYR A 6 106.113 -6.641 4.429 1.00 41.85 C
ATOM 57 CD1 TYR A 6 107.060 -7.067 5.358 1.00 41.58 C
ATOM 58 CD2 TYR A 6 106.485 -5.657 3.514 1.00 42.68 C
ATOM 59 CE1 TYR A 6 108.354 -6.529 5.370 1.00 42.16 C
ATOM 60 CE2 TYR A 6 107.771 -5.118 3.518 1.00 42.37 C
ATOM 61 CZ TYR A 6 108.698 -5.561 4.447 1.00 43.45 C
ATOM 62 OH TYR A 6 109.970 -5.038 4.439 1.00 47.92 O
ATOM 63 H TYR A 6 104.207 -8.092 6.928 1.00 0.00 H
ATOM 64 HH TYR A 6 110.053 -4.372 3.762 1.00 0.00 H
ATOM 65 N PHE A 7 101.785 -6.598 4.061 1.00 33.52 N
ATOM 66 CA PHE A 7 100.457 -7.008 3.674 1.00 31.78 C
ATOM 67 C PHE A 7 100.422 -6.936 2.188 1.00 34.65 C
ATOM 68 O PHE A 7 100.499 -5.842 1.624 1.00 38.88 O
ATOM 69 CB PHE A 7 99.438 -6.054 4.239 1.00 29.64 C
ATOM 70 CG PHE A 7 99.519 -5.916 5.713 1.00 29.53 C
ATOM 71 CD1 PHE A 7 100.401 -5.020 6.281 1.00 33.06 C
ATOM 72 CD2 PHE A 7 98.744 -6.708 6.542 1.00 29.50 C
ATOM 73 CE1 PHE A 7 100.512 -4.915 7.655 1.00 32.72 C
ATOM 74 CE2 PHE A 7 98.845 -6.611 7.927 1.00 25.38 C
ATOM 75 CZ PHE A 7 99.730 -5.714 8.481 1.00 31.43 C
ATOM 76 H PHE A 7 102.238 -5.873 3.563 1.00 0.00 H
ATOM 77 N HIS A 8 100.369 -8.098 1.549 1.00 33.28 N
ATOM 78 CA HIS A 8 100.339 -8.142 0.116 1.00 31.09 C
ATOM 79 C HIS A 8 98.947 -8.463 -0.339 1.00 32.15 C
ATOM 80 O HIS A 8 98.291 -9.308 0.246 1.00 31.62 O
ATOM 81 CB HIS A 8 101.268 -9.209 -0.355 1.00 31.37 C
ATOM 82 CG HIS A 8 102.558 -9.238 0.391 1.00 35.09 C
ATOM 83 ND1 HIS A 8 103.678 -8.558 -0.031 1.00 33.55 N
ATOM 84 CD2 HIS A 8 102.926 -9.924 1.500 1.00 35.89 C
ATOM 85 CE1 HIS A 8 104.683 -8.826 0.785 1.00 38.90 C
ATOM 86 NE2 HIS A 8 104.254 -9.655 1.721 1.00 35.13 N
ATOM 87 H HIS A 8 100.379 -8.933 2.051 1.00 0.00 H
ATOM 88 HD1 HIS A 8 103.753 -8.060 -0.857 1.00 0.00 H
ATOM 89 HE2 HIS A 8 104.773 -9.977 2.483 1.00 0.00 H
ATOM 90 N THR A 9 98.524 -7.819 -1.421 1.00 33.13 N
ATOM 91 CA THR A 9 97.197 -8.008 -1.965 1.00 33.45 C
ATOM 92 C THR A 9 97.290 -8.092 -3.464 1.00 38.82 C
ATOM 93 O THR A 9 98.000 -7.297 -4.102 1.00 42.52 O
ATOM 94 CB THR A 9 96.312 -6.806 -1.633 1.00 33.62 C
ATOM 95 OG1 THR A 9 95.989 -6.826 -0.239 1.00 38.90 O
ATOM 96 CG2 THR A 9 95.028 -6.810 -2.468 1.00 23.49 C
ATOM 97 H THR A 9 99.148 -7.215 -1.872 1.00 0.00 H
ATOM 98 HG1 THR A 9 95.474 -6.063 0.035 1.00 0.00 H
ATOM 99 N SER A 10 96.528 -9.013 -4.041 1.00 39.17 N
ATOM 100 CA SER A 10 96.534 -9.191 -5.475 1.00 36.48 C
ATOM 101 C SER A 10 95.105 -9.321 -5.916 1.00 36.12 C
ATOM 102 O SER A 10 94.339 -10.096 -5.341 1.00 39.87 O
ATOM 103 CB SER A 10 97.309 -10.446 -5.848 1.00 38.36 C
ATOM 104 OG SER A 10 97.596 -10.451 -7.241 1.00 42.16 O
ATOM 105 H SER A 10 95.942 -9.559 -3.476 1.00 0.00 H
ATOM 106 HG SER A 10 98.090 -11.245 -7.468 1.00 0.00 H
ATOM 107 N VAL A 11 94.736 -8.558 -6.934 1.00 36.19 N
ATOM 108 CA VAL A 11 93.377 -8.572 -7.431 1.00 36.54 C
ATOM 109 C VAL A 11 93.358 -8.771 -8.920 1.00 38.98 C
ATOM 110 O VAL A 11 93.985 -8.028 -9.668 1.00 39.07 O
ATOM 111 CB VAL A 11 92.696 -7.257 -7.114 1.00 33.80 C
ATOM 112 CG1 VAL A 11 91.322 -7.218 -7.741 1.00 36.28 C
ATOM 113 CG2 VAL A 11 92.614 -7.078 -5.624 1.00 29.08 C
ATOM 114 H VAL A 11 95.382 -7.964 -7.362 1.00 0.00 H
ATOM 115 N SER A 12 92.586 -9.748 -9.348 1.00 44.12 N
ATOM 116 CA SER A 12 92.491 -10.058 -10.751 1.00 52.21 C
ATOM 117 C SER A 12 91.612 -9.073 -11.486 1.00 56.63 C
ATOM 118 O SER A 12 90.635 -8.566 -10.941 1.00 55.16 O
ATOM 119 CB SER A 12 91.899 -11.439 -10.905 1.00 51.86 C
ATOM 120 OG SER A 12 90.572 -11.435 -10.418 1.00 60.85 O
ATOM 121 H SER A 12 92.067 -10.266 -8.706 1.00 0.00 H
ATOM 122 HG SER A 12 90.242 -12.339 -10.466 1.00 0.00 H
ATOM 123 N ARG A 13 91.966 -8.827 -12.739 1.00 65.15 N
ATOM 124 CA ARG A 13 91.213 -7.936 -13.609 1.00 74.06 C
ATOM 125 C ARG A 13 91.089 -8.779 -14.859 1.00 79.03 C
ATOM 126 O ARG A 13 92.098 -9.204 -15.420 1.00 82.84 O
ATOM 127 CB ARG A 13 92.013 -6.671 -13.907 1.00 75.51 C
ATOM 128 CG ARG A 13 92.542 -5.994 -12.658 1.00 83.43 C
ATOM 129 CD ARG A 13 94.032 -5.704 -12.778 1.00 90.70 C
ATOM 130 NE ARG A 13 94.284 -4.604 -13.702 1.00 97.00 N
ATOM 131 CZ ARG A 13 94.964 -3.506 -13.385 1.00 99.93 C
ATOM 132 NH1 ARG A 13 95.480 -3.367 -12.170 1.00100.00 N
ATOM 133 NH2 ARG A 13 95.058 -2.509 -14.260 1.00100.00 N
ATOM 134 H ARG A 13 92.779 -9.264 -13.089 1.00 0.00 H
ATOM 135 HE ARG A 13 93.941 -4.685 -14.615 1.00 0.00 H
ATOM 136 HH11 ARG A 13 95.370 -4.084 -11.483 1.00 0.00 H
ATOM 137 HH12 ARG A 13 95.977 -2.532 -11.941 1.00 0.00 H
ATOM 138 HH21 ARG A 13 94.611 -2.591 -15.151 1.00 0.00 H
ATOM 139 HH22 ARG A 13 95.551 -1.672 -14.023 1.00 0.00 H
ATOM 140 N PRO A 14 89.855 -9.092 -15.276 1.00 81.30 N
ATOM 141 CA PRO A 14 89.620 -9.908 -16.468 1.00 83.27 C
ATOM 142 C PRO A 14 90.051 -9.144 -17.705 1.00 87.37 C
ATOM 143 O PRO A 14 90.970 -9.552 -18.428 1.00 87.01 O
ATOM 144 CB PRO A 14 88.105 -10.084 -16.467 1.00 81.58 C
ATOM 145 CG PRO A 14 87.720 -9.830 -15.040 1.00 81.17 C
ATOM 146 CD PRO A 14 88.581 -8.674 -14.683 1.00 78.88 C
ATOM 147 N GLY A 15 89.417 -7.991 -17.892 1.00 90.13 N
ATOM 148 CA GLY A 15 89.699 -7.159 -19.044 1.00 93.50 C
ATOM 149 C GLY A 15 91.082 -6.548 -19.108 1.00 94.63 C
ATOM 150 O GLY A 15 91.786 -6.701 -20.106 1.00 96.79 O
ATOM 151 H GLY A 15 88.754 -7.714 -17.235 1.00 0.00 H
ATOM 152 N ARG A 16 91.498 -5.914 -18.022 1.00 94.03 N
ATOM 153 CA ARG A 16 92.783 -5.239 -17.975 1.00 92.59 C
ATOM 154 C ARG A 16 94.022 -6.119 -17.861 1.00 90.79 C
ATOM 155 O ARG A 16 95.065 -5.664 -17.393 1.00 91.34 O
ATOM 156 CB ARG A 16 92.763 -4.194 -16.859 1.00 96.07 C
ATOM 157 CG ARG A 16 91.997 -2.915 -17.218 1.00100.00 C
ATOM 158 CD ARG A 16 90.577 -3.187 -17.759 1.00100.00 C
ATOM 159 NE ARG A 16 89.524 -2.932 -16.773 1.00100.00 N
ATOM 160 CZ ARG A 16 88.852 -3.876 -16.116 1.00100.00 C
ATOM 161 NH1 ARG A 16 89.118 -5.163 -16.328 1.00100.00 N
ATOM 162 NH2 ARG A 16 87.896 -3.529 -15.254 1.00100.00 N
ATOM 163 H ARG A 16 90.958 -5.921 -17.205 1.00 0.00 H
ATOM 164 HE ARG A 16 89.311 -1.989 -16.569 1.00 0.00 H
ATOM 165 HH11 ARG A 16 89.836 -5.401 -16.975 1.00 0.00 H
ATOM 166 HH12 ARG A 16 88.627 -5.872 -15.822 1.00 0.00 H
ATOM 167 HH21 ARG A 16 87.660 -2.563 -15.125 1.00 0.00 H
ATOM 168 HH22 ARG A 16 87.384 -4.239 -14.770 1.00 0.00 H
ATOM 169 N GLY A 17 93.922 -7.368 -18.297 1.00 88.18 N
ATOM 170 CA GLY A 17 95.073 -8.249 -18.229 1.00 85.91 C
ATOM 171 C GLY A 17 95.641 -8.454 -16.831 1.00 85.95 C
ATOM 172 O GLY A 17 94.897 -8.737 -15.885 1.00 90.03 O
ATOM 173 H GLY A 17 93.084 -7.707 -18.673 1.00 0.00 H
ATOM 174 N GLU A 18 96.950 -8.263 -16.702 1.00 81.56 N
ATOM 175 CA GLU A 18 97.684 -8.449 -15.443 1.00 75.32 C
ATOM 176 C GLU A 18 97.023 -7.922 -14.158 1.00 68.95 C
ATOM 177 O GLU A 18 96.658 -6.752 -14.062 1.00 67.11 O
ATOM 178 CB GLU A 18 99.086 -7.879 -15.603 1.00 77.47 C
ATOM 179 CG GLU A 18 100.031 -8.264 -14.503 1.00 84.54 C
ATOM 180 CD GLU A 18 101.469 -8.006 -14.881 1.00 88.71 C
ATOM 181 OE1 GLU A 18 101.923 -6.849 -14.711 1.00 87.82 O
ATOM 182 OE2 GLU A 18 102.134 -8.961 -15.358 1.00 90.94 O
ATOM 183 H GLU A 18 97.448 -7.991 -17.501 1.00 0.00 H
ATOM 184 N PRO A 19 96.900 -8.785 -13.135 1.00 63.11 N
ATOM 185 CA PRO A 19 96.288 -8.464 -11.849 1.00 59.41 C
ATOM 186 C PRO A 19 96.994 -7.368 -11.068 1.00 54.94 C
ATOM 187 O PRO A 19 98.221 -7.300 -11.061 1.00 54.56 O
ATOM 188 CB PRO A 19 96.368 -9.789 -11.098 1.00 57.87 C
ATOM 189 CG PRO A 19 97.633 -10.346 -11.586 1.00 56.43 C
ATOM 190 CD PRO A 19 97.481 -10.138 -13.077 1.00 60.12 C
ATOM 191 N ARG A 20 96.201 -6.564 -10.377 1.00 50.06 N
ATOM 192 CA ARG A 20 96.705 -5.471 -9.565 1.00 47.00 C
ATOM 193 C ARG A 20 97.437 -6.076 -8.394 1.00 41.72 C
ATOM 194 O ARG A 20 96.958 -7.023 -7.803 1.00 43.58 O
ATOM 195 CB ARG A 20 95.536 -4.651 -9.022 1.00 52.17 C
ATOM 196 CG ARG A 20 95.795 -3.158 -8.948 1.00 58.51 C
ATOM 197 CD ARG A 20 96.908 -2.835 -7.977 1.00 64.18 C
ATOM 198 NE ARG A 20 97.290 -1.425 -8.010 1.00 71.56 N
ATOM 199 CZ ARG A 20 96.488 -0.422 -7.676 1.00 72.53 C
ATOM 200 NH1 ARG A 20 95.249 -0.661 -7.279 1.00 74.18 N
ATOM 201 NH2 ARG A 20 96.933 0.825 -7.733 1.00 77.74 N
ATOM 202 H ARG A 20 95.240 -6.706 -10.399 1.00 0.00 H
ATOM 203 HE ARG A 20 98.204 -1.211 -8.286 1.00 0.00 H
ATOM 204 HH11 ARG A 20 94.910 -1.599 -7.211 1.00 0.00 H
ATOM 205 HH12 ARG A 20 94.650 0.102 -7.037 1.00 0.00 H
ATOM 206 HH21 ARG A 20 97.870 1.011 -8.022 1.00 0.00 H
ATOM 207 HH22 ARG A 20 96.333 1.589 -7.496 1.00 0.00 H
ATOM 208 N PHE A 21 98.584 -5.523 -8.036 1.00 38.89 N
ATOM 209 CA PHE A 21 99.325 -6.061 -6.905 1.00 36.15 C
ATOM 210 C PHE A 21 99.925 -4.959 -6.048 1.00 37.49 C
ATOM 211 O PHE A 21 100.630 -4.087 -6.560 1.00 42.06 O
ATOM 212 CB PHE A 21 100.434 -6.975 -7.374 1.00 31.78 C
ATOM 213 CG PHE A 21 101.294 -7.478 -6.259 1.00 32.25 C
ATOM 214 CD1 PHE A 21 102.406 -6.768 -5.849 1.00 35.51 C
ATOM 215 CD2 PHE A 21 100.979 -8.654 -5.597 1.00 33.28 C
ATOM 216 CE1 PHE A 21 103.208 -7.225 -4.783 1.00 36.45 C
ATOM 217 CE2 PHE A 21 101.774 -9.125 -4.527 1.00 33.81 C
ATOM 218 CZ PHE A 21 102.891 -8.406 -4.121 1.00 33.73 C
ATOM 219 H PHE A 21 98.932 -4.735 -8.508 1.00 0.00 H
ATOM 220 N ILE A 22 99.791 -5.094 -4.732 1.00 33.28 N
ATOM 221 CA ILE A 22 100.272 -4.071 -3.820 1.00 28.83 C
ATOM 222 C ILE A 22 100.867 -4.632 -2.552 1.00 30.81 C
ATOM 223 O ILE A 22 100.282 -5.506 -1.923 1.00 34.51 O
ATOM 224 CB ILE A 22 99.102 -3.212 -3.382 1.00 26.79 C
ATOM 225 CG1 ILE A 22 98.446 -2.580 -4.597 1.00 27.20 C
ATOM 226 CG2 ILE A 22 99.560 -2.146 -2.432 1.00 27.22 C
ATOM 227 CD1 ILE A 22 97.202 -1.811 -4.272 1.00 28.69 C
ATOM 228 H ILE A 22 99.373 -5.900 -4.370 1.00 0.00 H
ATOM 229 N SER A 23 101.998 -4.087 -2.135 1.00 32.28 N
ATOM 230 CA SER A 23 102.631 -4.534 -0.906 1.00 35.47 C
ATOM 231 C SER A 23 102.917 -3.319 -0.074 1.00 36.24 C
ATOM 232 O SER A 23 103.264 -2.278 -0.616 1.00 41.24 O
ATOM 233 CB SER A 23 103.961 -5.214 -1.188 1.00 35.55 C
ATOM 234 OG SER A 23 103.770 -6.465 -1.819 1.00 45.62 O
ATOM 235 H SER A 23 102.414 -3.366 -2.654 1.00 0.00 H
ATOM 236 HG SER A 23 104.610 -6.916 -1.969 1.00 0.00 H
ATOM 237 N VAL A 24 102.757 -3.437 1.236 1.00 35.37 N
ATOM 238 CA VAL A 24 103.028 -2.333 2.127 1.00 34.72 C
ATOM 239 C VAL A 24 103.660 -2.915 3.366 1.00 38.62 C
ATOM 240 O VAL A 24 103.292 -4.023 3.811 1.00 40.50 O
ATOM 241 CB VAL A 24 101.749 -1.575 2.518 1.00 35.67 C
ATOM 242 CG1 VAL A 24 100.993 -1.156 1.271 1.00 36.34 C
ATOM 243 CG2 VAL A 24 100.849 -2.423 3.409 1.00 35.03 C
ATOM 244 H VAL A 24 102.456 -4.296 1.609 1.00 0.00 H
ATOM 245 N GLY A 25 104.635 -2.189 3.903 1.00 39.69 N
ATOM 246 CA GLY A 25 105.324 -2.645 5.089 1.00 40.46 C
ATOM 247 C GLY A 25 105.100 -1.728 6.267 1.00 42.12 C
ATOM 248 O GLY A 25 104.986 -0.505 6.130 1.00 42.92 O
ATOM 249 H GLY A 25 104.901 -1.341 3.487 1.00 0.00 H
ATOM 250 N TYR A 26 105.132 -2.310 7.450 1.00 42.93 N
ATOM 251 CA TYR A 26 104.918 -1.546 8.652 1.00 43.88 C
ATOM 252 C TYR A 26 105.833 -1.949 9.772 1.00 45.74 C
ATOM 253 O TYR A 26 106.244 -3.108 9.880 1.00 45.38 O
ATOM 254 CB TYR A 26 103.519 -1.792 9.179 1.00 44.85 C
ATOM 255 CG TYR A 26 102.410 -1.070 8.484 1.00 44.70 C
ATOM 256 CD1 TYR A 26 101.759 -1.639 7.402 1.00 44.75 C
ATOM 257 CD2 TYR A 26 101.926 0.134 8.987 1.00 46.17 C
ATOM 258 CE1 TYR A 26 100.636 -1.032 6.844 1.00 49.84 C
ATOM 259 CE2 TYR A 26 100.808 0.750 8.438 1.00 46.67 C
ATOM 260 CZ TYR A 26 100.167 0.161 7.369 1.00 48.84 C
ATOM 261 OH TYR A 26 99.047 0.747 6.821 1.00 51.30 O
ATOM 262 H TYR A 26 105.305 -3.266 7.504 1.00 0.00 H
ATOM 263 HH TYR A 26 98.784 0.282 6.021 1.00 0.00 H
ATOM 264 N VAL A 27 106.132 -0.978 10.620 1.00 47.40 N
ATOM 265 CA VAL A 27 106.902 -1.236 11.813 1.00 50.29 C
ATOM 266 C VAL A 27 105.941 -0.665 12.832 1.00 50.72 C